ID D0VEX7_ECOLI Unreviewed; 308 AA.
AC D0VEX7;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Arabinose 5-phosphate isomerase {ECO:0000256|PIRNR:PIRNR004692};
DE Short=API {ECO:0000256|PIRNR:PIRNR004692};
DE EC=5.3.1.13 {ECO:0000256|PIRNR:PIRNR004692};
GN Name=gutQ {ECO:0000313|EMBL:ACY27492.1};
OS Escherichia coli LW1655F+.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=527799 {ECO:0000313|EMBL:ACY27492.1};
RN [1] {ECO:0000313|EMBL:ACY27492.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LW1655F+ {ECO:0000313|EMBL:ACY27492.1};
RA Keanov D., Kaleta C., Petzold A., Hoischen C., Diekmann S., Siddiqui R.,
RA Schuster S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACY27492.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LW1655F+ {ECO:0000313|EMBL:ACY27492.1};
RX PubMed=20088879; DOI=10.1111/j.1742-4658.2009.07546.x;
RA Kenanov D., Kaleta C., Petzold A., Hoischen C., Diekmann S., Siddiqui R.A.,
RA Schuster S.;
RT "Theoretical study of lipid biosynthesis in wild-type Escherichia coli and
RT in a protoplast-type L-form using elementary flux mode analysis.";
RL FEBS J. 277:1023-1034(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121;
CC EC=5.3.1.13; Evidence={ECO:0000256|PIRNR:PIRNR004692};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000256|ARBA:ARBA00008165, ECO:0000256|PIRNR:PIRNR004692}.
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DR EMBL; GU072603; ACY27492.1; -; Genomic_DNA.
DR AlphaFoldDB; D0VEX7; -.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04604; CBS_pair_SIS_assoc; 1.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR NCBIfam; TIGR00393; kpsF; 1.
DR PANTHER; PTHR42745; -; 1.
DR PANTHER; PTHR42745:SF2; ARABINOSE 5-PHOSPHATE ISOMERASE GUTQ; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Isomerase {ECO:0000256|PIRNR:PIRNR004692, ECO:0000313|EMBL:ACY27492.1};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 21..164
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 190..248
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 256..308
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 39
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 91
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 132
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 173
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 308 AA; 32646 MW; ADD0F09314734163 CRC64;
MLELQEASRL PERLGDDFVR AANIILHCEG KVVVSGIGKS GHIGKKIAAT LASTGTPAFF
VHPAEALHGD LGMIESRDVM LFISYSGGAK ELDLIIPRLE DKSIALLAMT GKPTSPLGLA
AKAVLDISVE REACPMHLAP TSSTVNTLMM GDALAMAVMQ ARGFNEEDFA RSHPAGALGA
RLLNKVHHLM RRDDAIPQVA LTASVMDAML ELSRTGLGLV AVCDAQQQVQ GVFTDGDLRR
WLVGGGALTT PVNEAMTVGG TTLQSQSRAI DAKEILMKRK ITAAPVVDEN GKLTGAINLQ
DFYQAGII
//
